Angiotensin I-converting enzyme

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Angiotensin I-converting enzyme
[[Image:{{{Image}}}|thumb|220px|2D structure for Angiotensin I-converting enzyme]]
Chemical Name
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Chemical Information
Biochemical Taxonomy
Functional Taxonomy
Nutritional Taxonomy
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Biofluid Location
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Abnormal Biofluid Concentrations
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Authors: L. Pellis
Affiliations: TNO, the Netherlands


Contents

Introduction

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The angiotensins are peptides that act as vasoconstricting agents. ACE converts angiotensin to its activated form (called angiotensin II) enabling it to function. ACE is also involved it is involved in the inactivation of bradykinin, a potent vasodilator. These two actions make ACE an ideal target in the treatment of conditions such as high blood pressure, heart failure, diabetic nephropathy and type 2 diabetes mellitus. Inhibition of ACE results in decreased formation of Angiotensin II (a far more potent vasoconstrictor than Angiotensin I) and decreased inactivation of bradykinin.

Biological Function

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Angiotensin I-converting enzyme (EC 3.4.15.1), or kininase II, is a dipeptidyl carboxypeptidase that plays an important role in blood pressure regulation and electrolyte balance by hydrolyzing angiotensin I into angiotensin II, a potent vasopressor, and aldosterone-stimulating peptide. The enzyme is also able to inactivate bradykinin, a potent vasodilator.

Catabolism

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Diseases / Conditions Related to Nutrition

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Associated decreased protein/metabolite profile

Associated increased protein/metabolite profile

Other (Monogenic) Disorders

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Nutritional Information

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Drivers for biological variation

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Vulnerable groups

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Other resources

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Links

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OMIM

UniProtKB